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α/β-Peptide Foldamers Targeting Intracellular Protein–Protein Interactions with Activity in Living Cells

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† †Department of Chemistry, ⊥Department of Biomedical Engineering, ∥Department of Biochemistry, and ∇Department of Orthopedics and Rehabilitation, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States
‡ The Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria 3052, Australia
§ Department of Medical Biology, University of Melbourne, Parkville, Victoria 3010, Australia
◆ Department of Chemistry and Physics, La Trobe Institute of Molecular Science, Melbourne, Victoria 3086, Australia
*[email protected]
*[email protected]
Cite this: J. Am. Chem. Soc. 2015, 137, 35, 11365–11375
Publication Date (Web):August 28, 2015
https://doi.org/10.1021/jacs.5b05896
Copyright © 2015 American Chemical Society
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    Peptides can be developed as effective antagonists of protein–protein interactions, but conventional peptides (i.e., oligomers of l-α-amino acids) suffer from significant limitations in vivo. Short half-lives due to rapid proteolytic degradation and an inability to cross cell membranes often preclude biological applications of peptides. Oligomers that contain both α- and β-amino acid residues (“α/β-peptides”) manifest decreased susceptibility to proteolytic degradation, and when properly designed these unnatural oligomers can mimic the protein-recognition properties of analogous “α-peptides”. This report documents an extension of the α/β-peptide approach to target intracellular protein–protein interactions. Specifically, we have generated α/β-peptides based on a “stapled” Bim BH3 α-peptide, which contains a hydrocarbon cross-link to enhance α-helix stability. We show that a stapled α/β-peptide can structurally and functionally mimic the parent stapled α-peptide in its ability to enter certain types of cells and block protein–protein interactions associated with apoptotic signaling. However, the α/β-peptide is nearly 100-fold more resistant to proteolysis than is the parent stapled α-peptide. These results show that backbone modification, a strategy that has received relatively little attention in terms of peptide engineering for biomedical applications, can be combined with more commonly deployed peripheral modifications such as side chain cross-linking to produce synergistic benefits.

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